Biophysical characterization of Ca2+-binding of S100A5 and Ca2+-induced interaction with RAGE.
Biochem Biophys Res Commun
; 483(1): 332-338, 2017 01 29.
Article
in En
| MEDLINE
| ID: mdl-28017722
ABSTRACT
S100A5 is a calcium-binding protein of S100 family, which represents a major ligand to the receptor for advanced glycation end product (RAGE), a pattern recognition receptor engaged in diverse pathological processes. Here we have characterized calcium binding of S100A5 and the complex formation between S100A5 and RAGE using calorimetry and NMR spectroscopy. S100A5 binds to calcium ions in a sequential manner with the equilibrium dissociation constants (KD) of 1.3 µM and 3.5 µM, which corresponds to the calcium-binding at the C-terminal and N-terminal EF-hands. Upon calcium binding, S100A5 interacts with the V domain of RAGE (RAGE-v) to form a heterotrimer (KD â¼5.9 µM) that is distinct among the S100 family proteins. Chemical shift perturbation data from NMR titration experiments indicates that S100A5 employs the periphery of the dimer interface to interact with RAGE-v. Distinct binding mode and stoichiometry of RAGE against different S100 family proteins could be important to modulate diverse RAGE signaling.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
S100 Proteins
/
Calcium
/
Mitogen-Activated Protein Kinases
/
Antigens, Neoplasm
Limits:
Humans
Language:
En
Journal:
Biochem Biophys Res Commun
Year:
2017
Type:
Article